Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Bromodomain adjacent to zinc finger domain protein 1A (ATP-dependent chromatin-remodeling protein) (ATP-utilizing chromatin assembly and remodeling factor 1) (hACF1) (CHRAC subunit ACF1) (Williams syndrome transcription factor-related chromatin-remodeling factor 180) (WCRF180) (hWALp1)

 BAZ1A_HUMAN             Reviewed;        1556 AA.
Q9NRL2; Q9NZ15; Q9P065; Q9UIG1; Q9Y3V3;
30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
25-OCT-2017, entry version 176.
RecName: Full=Bromodomain adjacent to zinc finger domain protein 1A;
AltName: Full=ATP-dependent chromatin-remodeling protein;
AltName: Full=ATP-utilizing chromatin assembly and remodeling factor 1;
Short=hACF1;
AltName: Full=CHRAC subunit ACF1;
AltName: Full=Williams syndrome transcription factor-related chromatin-remodeling factor 180;
Short=WCRF180;
AltName: Full=hWALp1;
Name=BAZ1A; Synonyms=ACF1, WCRF180; ORFNames=HSPC317;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS
SPECTROMETRY, IDENTIFICATION IN THE CHRAC COMPLEX, AND VARIANT
LYS-1366.
TISSUE=Cervix carcinoma;
PubMed=10880450; DOI=10.1093/emboj/19.13.3377;
Poot R.A., Dellaire G., Huelsmann B.B., Grimaldi M.A., Corona D.F.V.,
Becker P.B., Bickmore W.A., Varga-Weisz P.D.;
"HuCHRAC, a human ISWI chromatin remodelling complex contains hACF1
and two novel histone-fold proteins.";
EMBO J. 19:3377-3387(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=10655480; DOI=10.1073/pnas.97.3.1038;
Bochar D.A., Savard J., Wang W., Lafleur D.W., Moore P., Cote J.,
Shiekhattar R.;
"A family of chromatin remodeling factors related to Williams syndrome
transcription factor.";
Proc. Natl. Acad. Sci. U.S.A. 97:1038-1043(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=10662543; DOI=10.1006/geno.1999.6071;
Jones M.H., Hamana N., Nezu J., Shimane M.;
"A novel family of bromodomain genes.";
Genomics 63:40-45(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-540 (ISOFORM 1).
TISSUE=Umbilical cord blood;
Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
"Human partial CDS from CD34+ stem cells.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 746-1556 (ISOFORM 1), AND
VARIANT LYS-1366.
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
FUNCTION, AND INTERACTION WITH SMARCA5 IN THE AFC COMPLEX.
PubMed=12434153; DOI=10.1038/ng1046;
Collins N., Poot R.A., Kukimoto I., Garcia-Jimenez C., Dellaire G.,
Varga-Weisz P.D.;
"An ACF1-ISWI chromatin-remodeling complex is required for DNA
replication through heterochromatin.";
Nat. Genet. 32:627-632(2002).
[9]
ASSOCIATION WITH THE CHRAC1/POLE3 COMPLEX, AND FUNCTION OF THE CHRAC
COMPLEX.
PubMed=14759371; DOI=10.1016/S1097-2765(03)00523-9;
Kukimoto I., Elderkin S., Grimaldi M., Oelgeschlager T.,
Varga-Weisz P.D.;
"The histone-fold protein complex CHRAC-15/17 enhances nucleosome
sliding and assembly mediated by ACF.";
Mol. Cell 13:265-277(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1413 AND SER-1417, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
FUNCTION OF ACF COMPLEX.
PubMed=17099699; DOI=10.1038/nsmb1170;
Yang J.G., Madrid T.S., Sevastopoulos E., Narlikar G.J.;
"The chromatin-remodeling enzyme ACF is an ATP-dependent DNA length
sensor that regulates nucleosome spacing.";
Nat. Struct. Mol. Biol. 13:1078-1083(2006).
[12]
INTERACTION WITH NCOR1, AND POSSIBLE FUNCTION.
PubMed=17519354; DOI=10.1210/me.2007-0095;
Ewing A.K., Attner M., Chakravarti D.;
"Novel regulatory role for human Acf1 in transcriptional repression of
vitamin D3 receptor-regulated genes.";
Mol. Endocrinol. 21:1791-1806(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1402; SER-1413 AND
SER-1417, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270 AND SER-702, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270; SER-1371 AND
SER-1402, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-731; SER-1281 AND
SER-1413, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-731; SER-961; SER-1281;
SER-1320; SER-1363; SER-1413; SER-1417 AND THR-1547, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-952, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Component of the ACF complex, an ATP-dependent chromatin
remodeling complex, that regulates spacing of nucleosomes using
ATP to generate evenly spaced nucleosomes along the chromatin. The
ATPase activity of the complex is regulated by the length of
flanking DNA. Also involved in facilitating the DNA replication
process. BAZ1A is the accessory, non-catalytic subunit of the
complex which can enhance and direct the process provided by the
ATPase subunit, SMARCA5, probably through targeting
pericentromeric heterochromatin in late S phase. Moves end-
positioned nucleosomes to a predominantly central position. May
have a role in nuclear receptor-mediated transcription repression.
-!- FUNCTION: Component of the histone-fold protein complex CHRAC
complex which faciliates nucleosome sliding by the ACF complex and
enhances ACF-mediated chromatin assembly. The C-terminal regions
of both CHRAC1 and POLE1 are required for these functions.
-!- SUBUNIT: Component of the ACF chromatin remodeling complex that
includes BAZ1A and SMARCA5. Additional this complex can form,
together with CHRAC1 and POLE1, the histone-fold protein complex,
CHRAC. Interacts with NCOR1 (via its RD1 domain); the interaction
corepresses a number of NCOR1-regulated genes.
{ECO:0000269|PubMed:10880450, ECO:0000269|PubMed:12434153,
ECO:0000269|PubMed:17519354}.
-!- INTERACTION:
P42858:HTT; NbExp=4; IntAct=EBI-927511, EBI-466029;
O60264:SMARCA5; NbExp=3; IntAct=EBI-927511, EBI-352588;
O95365:ZBTB7A; NbExp=2; IntAct=EBI-927511, EBI-2795384;
-!- SUBCELLULAR LOCATION: Nucleus. Note=May target the CHRAC complex
to heterochromatin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NRL2-1; Sequence=Displayed;
Name=2;
IsoId=Q9NRL2-2; Sequence=VSP_000551;
-!- TISSUE SPECIFICITY: Highly expressed in testis and at low or
undetectable levels in other tissues analyzed.
-!- MISCELLANEOUS: Stimulated by double-stranded DNA and nucleosomal
DNA.
-!- SIMILARITY: Belongs to the WAL family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF28995.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF213467; AAF70601.1; -; mRNA.
EMBL; AF221130; AAF32366.1; -; mRNA.
EMBL; AB032252; BAA89209.1; -; mRNA.
EMBL; AL121603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL355885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471078; EAW65900.1; -; Genomic_DNA.
EMBL; AF161435; AAF28995.1; ALT_FRAME; mRNA.
EMBL; AL050089; CAB43261.1; -; mRNA.
CCDS; CCDS41943.1; -. [Q9NRL2-2]
CCDS; CCDS9651.1; -. [Q9NRL2-1]
PIR; T08738; T08738.
RefSeq; NP_038476.2; NM_013448.2. [Q9NRL2-1]
RefSeq; NP_872589.1; NM_182648.1. [Q9NRL2-2]
UniGene; Hs.509140; -.
PDB; 5UIY; X-ray; 1.69 A; A/B/C/D=1425-1538.
PDBsum; 5UIY; -.
ProteinModelPortal; Q9NRL2; -.
SMR; Q9NRL2; -.
BioGrid; 116347; 35.
CORUM; Q9NRL2; -.
DIP; DIP-36071N; -.
IntAct; Q9NRL2; 31.
MINT; MINT-1183777; -.
STRING; 9606.ENSP00000353458; -.
iPTMnet; Q9NRL2; -.
PhosphoSitePlus; Q9NRL2; -.
BioMuta; BAZ1A; -.
DMDM; 116241266; -.
EPD; Q9NRL2; -.
MaxQB; Q9NRL2; -.
PaxDb; Q9NRL2; -.
PeptideAtlas; Q9NRL2; -.
PRIDE; Q9NRL2; -.
Ensembl; ENST00000358716; ENSP00000351555; ENSG00000198604. [Q9NRL2-2]
Ensembl; ENST00000360310; ENSP00000353458; ENSG00000198604. [Q9NRL2-1]
Ensembl; ENST00000382422; ENSP00000371859; ENSG00000198604. [Q9NRL2-1]
GeneID; 11177; -.
KEGG; hsa:11177; -.
UCSC; uc001wsk.4; human. [Q9NRL2-1]
CTD; 11177; -.
DisGeNET; 11177; -.
EuPathDB; HostDB:ENSG00000198604.10; -.
GeneCards; BAZ1A; -.
H-InvDB; HIX0037904; -.
HGNC; HGNC:960; BAZ1A.
HPA; HPA002730; -.
MIM; 605680; gene.
neXtProt; NX_Q9NRL2; -.
OpenTargets; ENSG00000198604; -.
PharmGKB; PA25270; -.
eggNOG; KOG1245; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00760000119099; -.
HOGENOM; HOG000095179; -.
HOVERGEN; HBG080889; -.
InParanoid; Q9NRL2; -.
KO; K11655; -.
OMA; INSTVWQ; -.
OrthoDB; EOG091G06JE; -.
PhylomeDB; Q9NRL2; -.
TreeFam; TF316326; -.
ChiTaRS; BAZ1A; human.
GenomeRNAi; 11177; -.
PRO; PR:Q9NRL2; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000198604; -.
CleanEx; HS_BAZ1A; -.
ExpressionAtlas; Q9NRL2; baseline and differential.
Genevisible; Q9NRL2; HS.
GO; GO:0016590; C:ACF complex; TAS:BHF-UCL.
GO; GO:0008623; C:CHRAC; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006338; P:chromatin remodeling; TAS:BHF-UCL.
GO; GO:0006261; P:DNA-dependent DNA replication; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; NAS:BHF-UCL.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 3.30.40.10; -; 1.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR018501; DDT_dom.
InterPro; IPR032675; L_dom-like.
InterPro; IPR028942; WHIM1_dom.
InterPro; IPR028941; WHIM2_dom.
InterPro; IPR013136; WSTF_Acf1_Cbp146.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF02791; DDT; 1.
Pfam; PF00628; PHD; 1.
Pfam; PF10537; WAC_Acf1_DNA_bd; 1.
Pfam; PF15612; WHIM1; 1.
Pfam; PF15613; WSD; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 1.
SMART; SM00571; DDT; 1.
SMART; SM00249; PHD; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS50827; DDT; 1.
PROSITE; PS51136; WAC; 1.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Bromodomain; Coiled coil;
Complete proteome; Isopeptide bond; Metal-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 1556 Bromodomain adjacent to zinc finger
domain protein 1A.
/FTId=PRO_0000211167.
DOMAIN 22 128 WAC. {ECO:0000255|PROSITE-
ProRule:PRU00475}.
DOMAIN 422 487 DDT. {ECO:0000255|PROSITE-
ProRule:PRU00063}.
DOMAIN 1446 1516 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
ZN_FING 1148 1198 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
REGION 1 133 Required for interaction with NCOR1.
{ECO:0000269|PubMed:17519354}.
REGION 1 128 Required for association with the
CHRAC1/POLE3 complex.
REGION 667 933 Interaction with SMARCA5.
COILED 306 397 {ECO:0000255}.
COILED 634 709 {ECO:0000255}.
COMPBIAS 487 491 Poly-Glu.
COMPBIAS 1239 1257 Glu-rich.
MOD_RES 270 270 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 702 702 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 731 731 Phosphothreonine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 960 960 Phosphoserine.
{ECO:0000250|UniProtKB:O88379}.
MOD_RES 961 961 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1281 1281 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1320 1320 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1339 1339 Phosphoserine.
{ECO:0000250|UniProtKB:O88379}.
MOD_RES 1353 1353 Phosphoserine.
{ECO:0000250|UniProtKB:O88379}.
MOD_RES 1363 1363 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1371 1371 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1402 1402 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 1413 1413 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1417 1417 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1547 1547 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 952 952 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 504 535 Missing (in isoform 2).
{ECO:0000303|PubMed:10655480}.
/FTId=VSP_000551.
VARIANT 344 344 D -> E (in dbSNP:rs1133285).
/FTId=VAR_028049.
VARIANT 1366 1366 N -> K (in dbSNP:rs1044140).
{ECO:0000269|PubMed:10880450,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_048423.
CONFLICT 135 135 R -> T (in Ref. 3; BAA89209).
{ECO:0000305}.
CONFLICT 236 236 D -> E (in Ref. 3; BAA89209).
{ECO:0000305}.
CONFLICT 494 494 K -> Q (in Ref. 6; AAF28995).
{ECO:0000305}.
CONFLICT 503 508 KDLTEA -> QDFTEP (in Ref. 6; AAF28995).
{ECO:0000305}.
CONFLICT 525 525 S -> P (in Ref. 6; AAF28995).
{ECO:0000305}.
CONFLICT 536 540 GCSLK -> AALKF (in Ref. 6; AAF28995).
{ECO:0000305}.
CONFLICT 551 551 E -> D (in Ref. 1; AAF70601).
{ECO:0000305}.
CONFLICT 730 730 V -> F (in Ref. 3; BAA89209).
{ECO:0000305}.
CONFLICT 769 769 P -> L (in Ref. 3; BAA89209).
{ECO:0000305}.
CONFLICT 1201 1201 S -> C (in Ref. 3; BAA89209).
{ECO:0000305}.
CONFLICT 1206 1206 S -> F (in Ref. 3; BAA89209).
{ECO:0000305}.
CONFLICT 1409 1409 R -> K (in Ref. 1; AAF70601 and 7;
CAB43261). {ECO:0000305}.
SEQUENCE 1556 AA; 178702 MW; 4D78B9A8ADBF715B CRC64;
MPLLHRKPFV RQKPPADLRP DEEVFYCKVT NEIFRHYDDF FERTILCNSL VWSCAVTGRP
GLTYQEALES EKKARQNLQS FPEPLIIPVL YLTSLTHRSR LHEICDDIFA YVKDRYFVEE
TVEVIRNNGA RLQCRILEVL PPSHQNGFAN GHVNSVDGET IIISDSDDSE TQSCSFQNGK
KKDAIDPLLF KYKVQPTKKE LHESAIVKAT QISRRKHLFS RDKLKLFLKQ HCEPQDGVIK
IKASSLSTYK IAEQDFSYFF PDDPPTFIFS PANRRRGRPP KRIHISQEDN VANKQTLASY
RSKATKERDK LLKQEEMKSL AFEKAKLKRE KADALEAKKK EKEDKEKKRE ELKKIVEEER
LKKKEEKERL KVEREKEREK LREEKRKYVE YLKQWSKPRE DMECDDLKEL PEPTPVKTRL
PPEIFGDALM VLEFLNAFGE LFDLQDEFPD GVTLEVLEEA LVGNDSEGPL CELLFFFLTA
IFQAIAEEEE EVAKEQLTDA DTKDLTEALD EDADPTKSAL SAVASLAAAW PQLHQGCSLK
SLDLDSCTLS EILRLHILAS GADVTSANAK YRYQKRGGFD ATDDACMELR LSNPSLVKKL
SSTSVYDLTP GEKMKILHAL CGKLLTLVST RDFIEDYVDI LRQAKQEFRE LKAEQHRKER
EEAAARIRKR KEEKLKEQEQ KMKEKQEKLK EDEQRNSTAD ISIGEEERED FDTSIESKDT
EQKELDQDMV TEDEDDPGSH KRGRRGKRGQ NGFKEFTRQE QINCVTREPL TADEEEALKQ
EHQRKEKELL EKIQSAIACT NIFPLGRDRM YRRYWIFPSI PGLFIEEDYS GLTEDMLLPR
PSSFQNNVQS QDPQVSTKTG EPLMSESTSN IDQGPRDHSV QLPKPVHKPN RWCFYSSCEQ
LDQLIEALNS RGHRESALKE TLLQEKSRIC AQLARFSEEK FHFSDKPQPD SKPTYSRGRS
SNAYDPSQMC AEKQLELRLR DFLLDIEDRI YQGTLGAIKV TDRHIWRSAL ESGRYELLSE
ENKENGIIKT VNEDVEEMEI DEQTKVIVKD RLLGIKTETP STVSTNASTP QSVSSVVHYL
AMALFQIEQG IERRFLKAPL DASDSGRSYK TVLDRWRESL LSSASLSQVF LHLSTLDRSV
IWSKSILNAR CKICRKKGDA ENMVLCDGCD RGHHTYCVRP KLKTVPEGDW FCPECRPKQR
SRRLSSRQRP SLESDEDVED SMGGEDDEVD GDEEEGQSEE EEYEVEQDED DSQEEEEVSL
PKRGRPQVRL PVKTRGKLSS SFSSRGQQQE PGRYPSRSQQ STPKTTVSSK TGRSLRKINS
APPTETKSLR IASRSTRHSH GPLQADVFVE LLSPRRKRRG RKSANNTPEN SPNFPNFRVI
ATKSSEQSRS VNIASKLSLQ ESESKRRCRK RQSPEPSPVT LGRRSSGRQG GVHELSAFEQ
LVVELVRHDD SWPFLKLVSK IQVPDYYDII KKPIALNIIR EKVNKCEYKL ASEFIDDIEL
MFSNCFEYNP RNTSEAKAGT RLQAFFHIQA QKLGLHVTPS NVDQVSTPPA AKKSRI


Related products :

Catalog number Product name Quantity
EIAAB33908 CAF-1 subunit C,CAF-I 48 kDa subunit,CAF-I p48,Chromatin assembly factor 1 subunit C,Chromatin assembly factor I p48 subunit,Histone-binding protein RBBP4,Homo sapiens,Human,Nucleosome-remodeling fact
EIAAB33905 CAF-1 subunit C,CAF-I 48 kDa subunit,CAF-I p48,Chromatin assembly factor 1 subunit C,Chromatin assembly factor I p48 subunit,Histone-binding protein RBBP4,Mouse,Mus musculus,Nucleosome-remodeling fact
EIAAB36191 HBV pX-associated protein 8,HBXAP,Hepatitis B virus X-associated protein,Homo sapiens,Human,p325 subunit of RSF chromatin-remodeling complex,Remodeling and spacing factor 1,RSF1,Rsf-1,XAP8
EIAAB07147 AD-013,ATP-dependent helicase CHD9,CHD9,CHD-9,Chromatin-related mesenchymal modulator,Chromatin-remodeling factor CHROM1,Chromodomain-helicase-DNA-binding protein 9,CReMM,Homo sapiens,Human,KIAA0308,K
27-258 Brg- or hBrm-associated factor (BAF) complexes, a chromatin-remodeling complex family of mammalian cells, facilitate transcriptional activity by remodeling nucleosome structure. Brg1 is the core subun 0.05 mg
31-193 Brg- or hBrm-associated factor (BAF) complexes, a chromatin-remodeling complex family of mammalian cells, facilitate transcriptional activity by remodeling nucleosome structure. Brg1 is the core subun 0.1 mg
27-242 Brg- or hBrm-associated factor (BAF) complexes, a chromatin-remodeling complex family of mammalian cells, facilitate transcriptional activity by remodeling nucleosome structure. Brg1 is the core subun 0.05 mg
28-823 SMARCE1 is part of the large ATP-dependent chromatin remodeling complex SWI_SNF, which is required for transcriptional activation of genes normally repressed by chromatin. The protein, either alone or 0.05 mg
EIAAB33906 CAF-1 subunit C,CAF-I 48 kDa subunit,CAF-I p48,chCAF-1 p48,Chicken,Chromatin assembly factor 1 subunit C,Chromatin assembly factor I p48 subunit,Gallus gallus,Histone-binding protein RBBP4,RBAP48,RBBP
26-348 RSF1 (HBXAP) is involved in transcription repression, transcription coactivation when associated with hepatitis B virus X protein (HBX), and chromatin remodeling and spacing when associated with SNF2H 0.05 mg
EIAAB05139 CAF-1 subunit B,CAF1A,CAF1P60,CAF-I 60 kDa subunit,CAF-I p60,CHAF1B,Chromatin assembly factor 1 subunit B,Chromatin assembly factor I p60 subunit,Homo sapiens,Human,M-phase phosphoprotein 7,MPHOSPH7,M
30-704 MSL3L2 contains 1 chromo domain. It may be involved in chromatin remodeling and transcriptional regulation. 0.05 mg
26-579 MSL3L2 contains 1 chromo domain. It may be involved in chromatin remodeling and transcriptional regulation. 0.05 mg
EIAAB05135 CAF,CAF-1 subunit A,CAF1P150,CAF-I 150 kDa subunit,CAF-I p150,CHAF1A,Chromatin assembly factor 1 subunit A,Chromatin assembly factor I p150 subunit,Homo sapiens,hp150,Human
EIAAB40078 Chromatin-specific transcription elongation factor 80 kDa subunit,Facilitates chromatin transcription complex 80 kDa subunit,Facilitates chromatin transcription complex subunit SSRP1,FACT 80 kDa subun
EIAAB07249 CHRAC1,CHRAC-1,CHRAC15,CHRAC-15,Chromatin accessibility complex 15 kDa protein,Chromatin accessibility complex protein 1,DNA polymerase epsilon subunit p15,Homo sapiens,HuCHRAC15,Human
EIAAB05138 CAF-1 subunit B,CAF-I 60 kDa subunit,CAF-I p60,Chaf1b,Chromatin assembly factor 1 subunit B,Chromatin assembly factor I p60 subunit,Mouse,Mus musculus
EIAAB05137 CAF-1 subunit B,CAF1P60,CAF-I 60 kDa subunit,CAF-I p60,CHAF1B,Chicken,Chromatin assembly factor 1 subunit B,Chromatin assembly factor I p60 subunit,Gallus gallus,RCJMB04_5h12
EIAAB05136 Bos taurus,Bovine,CAF,CAF-1 subunit A,CAF1P150,CAF-I 150 kDa subunit,CAF-I p150,CHAF1A,Chromatin assembly factor 1 subunit A,Chromatin assembly factor I p150 subunit
EIAAB05133 CAF-1 subunit A,CAF-I 150 kDa subunit,CAF-I p150,Caip150,Chaf1a,Chromatin assembly factor 1 subunit A,Chromatin assembly factor I p150 subunit,Mouse,Mus musculus
29-130 MSL3L1 is a nuclear protein, which is thought to play a similar function in chromatin remodeling and transcriptional regulation. This gene has been found to undergo X inactivation. 0.1 mg
EIAAB05134 CAF-1 subunit A,CAF-I 150 kDa subunit,CAF-I p150,CAIP150,CHAF1A,Chicken,Chromatin assembly factor 1 subunit A,Chromatin assembly factor I p150 subunit,Gallus gallus,RCJMB04_12f19
25-498 PBRM1 is involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). 0.05 mg
25-553 MSL3L1 is a nuclear protein, which is thought to play a similar function in chromatin remodeling and transcriptional regulation. This gene has been found to undergo X inactivation. This gene encodes a 0.05 mg
EIAAB38774 ATP-dependent helicase SMARCA1,DNA-dependent ATPase SNF2L,Mouse,Mus musculus,Nucleosome-remodeling factor subunit SNF2L,Probable global transcription activator SNF2L1,Smarca1,Snf2l,SWI_SNF-related mat


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur